Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование
Novel protein from larval sponge cells, ilborin, is related to energy turnover and calcium binding and is conserved among marine invertebrates. / Borisenko, Ilya; Daugavet, Maria; Ereskovsky, Alexander; Lavrov, Andrey; Podgornaya, Olga.
в: Open Biology, Том 12, № 2, 210336, 23.02.2022.Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование
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TY - JOUR
T1 - Novel protein from larval sponge cells, ilborin, is related to energy turnover and calcium binding and is conserved among marine invertebrates
AU - Borisenko, Ilya
AU - Daugavet, Maria
AU - Ereskovsky, Alexander
AU - Lavrov, Andrey
AU - Podgornaya, Olga
N1 - Publisher Copyright: © 2022 Royal Society Publishing. All rights reserved.
PY - 2022/2/23
Y1 - 2022/2/23
N2 - Sponges (phylum Porifera) are early-branching animals, whose outwardly simple body plan is underlain by a complex genetic repertoire. The transition from a mobile larva to an attached filter-feeding organism occurs by metamorphosis, a process accompanied by a radical change of the body plan and cell transdifferentiation. The continuity between larval cells and adult tissues is still obscure. In a previous study, we have produced polyclonal antibodies against the major protein of the flagellated cells covering the larva of the sponge Halisarca dujardini, used them to trace the fate of these cells and shown that the larval flagellated cells transdifferentiate into the choanocytes. In the present work, we identified the sequence of this novel protein, which we named ilborin. A search in the open databases showed that multiple orthologues of the newly identified protein are present in sponges, cnidarians, flatworms, ctenophores and echinoderms, but none of them has been described yet. Ilborin has two conserved domains: Triosephosphate isomerase-barrel, which has enzymatic activity against macroergic compounds, and canonical EF-hand, which binds calcium. mRNA of ilborin is expressed in the larval flagellated cells. We suggest that the new protein is involved in the calcium-mediated regulation of energy metabolism, whose activation precedes metamorphosis.
AB - Sponges (phylum Porifera) are early-branching animals, whose outwardly simple body plan is underlain by a complex genetic repertoire. The transition from a mobile larva to an attached filter-feeding organism occurs by metamorphosis, a process accompanied by a radical change of the body plan and cell transdifferentiation. The continuity between larval cells and adult tissues is still obscure. In a previous study, we have produced polyclonal antibodies against the major protein of the flagellated cells covering the larva of the sponge Halisarca dujardini, used them to trace the fate of these cells and shown that the larval flagellated cells transdifferentiate into the choanocytes. In the present work, we identified the sequence of this novel protein, which we named ilborin. A search in the open databases showed that multiple orthologues of the newly identified protein are present in sponges, cnidarians, flatworms, ctenophores and echinoderms, but none of them has been described yet. Ilborin has two conserved domains: Triosephosphate isomerase-barrel, which has enzymatic activity against macroergic compounds, and canonical EF-hand, which binds calcium. mRNA of ilborin is expressed in the larval flagellated cells. We suggest that the new protein is involved in the calcium-mediated regulation of energy metabolism, whose activation precedes metamorphosis.
KW - Evolution
KW - Iarva
KW - Metamorphosis
KW - Porifera
KW - Protein
KW - Transdifferentiation
KW - HALISARCIDA
KW - MECHANISM
KW - MODULATED PROTEINS
KW - evolution
KW - ORGANISM
KW - EVOLUTION
KW - larva
KW - protein
KW - DYNAMICS
KW - transdifferentiation
KW - METAMORPHOSIS
KW - metamorphosis
KW - DEMOSPONGIAE
KW - HOMOLOGY
KW - PHOSPHOENOLPYRUVATE
UR - http://www.scopus.com/inward/record.url?scp=85125153786&partnerID=8YFLogxK
U2 - 10.1098/rsob.210336
DO - 10.1098/rsob.210336
M3 - Article
C2 - 35193395
VL - 12
JO - Open Biology
JF - Open Biology
SN - 2046-2441
IS - 2
M1 - 210336
ER -
ID: 92902824